BAIP2_MOUSE - dbPTM
BAIP2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BAIP2_MOUSE
UniProt AC Q8BKX1
Protein Name Brain-specific angiogenesis inhibitor 1-associated protein 2
Gene Name Baiap2
Organism Mus musculus (Mouse).
Sequence Length 535
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Cell projection, filopodium. Cell projection, ruffle. Cytoplasm, cytoskeleton. Detected throughout the cytoplasm in the absence of specific binding partners. Detected in filopodia and close to membran
Protein Description Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Participates in actin bundling when associated with EPS8, promoting filopodial protrusions..
Protein Sequence MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTFAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEETLKSFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPNKIPDRAVQLMQQMANSNGSILPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQENVPVMNGVAGPDSEDYNPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLALPPPDYGTSSRAFPTQTAGTFKQRPYSVAVPAFSQGLDDYGARSVSRNPFANVHLKPTVTNDRSAPLLS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSLSRSEEM
------CCCCHHHHH		34.7430635358
4Phosphorylation----MSLSRSEEMHR
----CCCCHHHHHHH		26.8430635358
6Phosphorylation--MSLSRSEEMHRLT
--CCCCHHHHHHHHH		34.2430635358
38PhosphorylationFIAMGKNYEKALAGV
HHHCCCCHHHHHHHH		23.4622871156
46PhosphorylationEKALAGVTFAAKGYF
HHHHHHHHHHHHHHH		13.4622871156
70UbiquitinationASESQGSKELGDVLF
HHCCCCCHHHHHHHH		64.88-
148PhosphorylationLKKLRKKSQGSKNPQ
HHHHHHHHCCCCCCC		42.6922345495
151PhosphorylationLRKKSQGSKNPQKYS
HHHHHCCCCCCCCCC		22.9422345495
171UbiquitinationYIDAISNKQGELENY
HHHHHHCCCCHHHHH		53.54-
235AcetylationQACADPNKIPDRAVQ
HHHCCCCCCCHHHHH		62.0922826441
250PhosphorylationLMQQMANSNGSILPS
HHHHHHHCCCCCCHH		32.7925619855
253PhosphorylationQMANSNGSILPSALS
HHHHCCCCCCHHHHH		25.7925619855
257PhosphorylationSNGSILPSALSASKS
CCCCCCHHHHHHCCC		38.0925619855
260PhosphorylationSILPSALSASKSNLV
CCCHHHHHHCCCCEE		30.1625619855
262PhosphorylationLPSALSASKSNLVIS
CHHHHHHCCCCEEEC		32.9925521595
264PhosphorylationSALSASKSNLVISDP
HHHHHCCCCEEECCC		32.6630352176
290 (in isoform 4)Phosphorylation-15.5826643407
292 (in isoform 4)Phosphorylation-25.9926643407
301 (in isoform 4)Phosphorylation-41.8630352176
324PhosphorylationRKAAQPKSLSPPQSQ
HHCCCCCCCCCCCHH		40.5425521595
326PhosphorylationAAQPKSLSPPQSQSK
CCCCCCCCCCCHHHH		41.4425521595
330PhosphorylationKSLSPPQSQSKLSDS
CCCCCCCHHHHCCCC		42.0424925903
332PhosphorylationLSPPQSQSKLSDSYS
CCCCCHHHHCCCCCC		40.5925777480
335PhosphorylationPQSQSKLSDSYSNTL
CCHHHHCCCCCCCCC		28.3925619855
337PhosphorylationSQSKLSDSYSNTLPV
HHHHCCCCCCCCCCC		27.3828973931
338PhosphorylationQSKLSDSYSNTLPVR
HHHCCCCCCCCCCCC		15.7825338131
339PhosphorylationSKLSDSYSNTLPVRK
HHCCCCCCCCCCCCC		27.5621082442
341PhosphorylationLSDSYSNTLPVRKSV
CCCCCCCCCCCCCCC		26.8826824392
347PhosphorylationNTLPVRKSVTPKNSY
CCCCCCCCCCCCCCC		22.2129514104
349PhosphorylationLPVRKSVTPKNSYAT
CCCCCCCCCCCCCCC		35.3229514104
351UbiquitinationVRKSVTPKNSYATTE
CCCCCCCCCCCCCCC		49.51-
353PhosphorylationKSVTPKNSYATTENK
CCCCCCCCCCCCCCC		23.4425619855
354PhosphorylationSVTPKNSYATTENKT
CCCCCCCCCCCCCCC		19.8425338131
356PhosphorylationTPKNSYATTENKTLP
CCCCCCCCCCCCCCC		26.8125619855
357PhosphorylationPKNSYATTENKTLPR
CCCCCCCCCCCCCCC		29.4125619855
360UbiquitinationSYATTENKTLPRSSS
CCCCCCCCCCCCCHH		45.25-
361PhosphorylationYATTENKTLPRSSSM
CCCCCCCCCCCCHHH		54.2826824392
365PhosphorylationENKTLPRSSSMAAGL
CCCCCCCCHHHHHHC		25.4827087446
366PhosphorylationNKTLPRSSSMAAGLE
CCCCCCCHHHHHHCH		25.9723984901
367PhosphorylationKTLPRSSSMAAGLER
CCCCCCHHHHHHCHH		17.4325521595
385PhosphorylationMRVKAIFSHAAGDNS
HHEEEEEECCCCCCC		13.2022324799
392PhosphorylationSHAAGDNSTLLSFKE
ECCCCCCCEEEEECC		25.7726239621
393PhosphorylationHAAGDNSTLLSFKEG
CCCCCCCEEEEECCC		37.6621183079
396PhosphorylationGDNSTLLSFKEGDLI
CCCCEEEEECCCCEE		37.0725521595
404PhosphorylationFKEGDLITLLVPEAR
ECCCCEEEEEEECCC		22.7226239621
441PhosphorylationRVLDSDGSDRLHMSL
EEECCCCCCCCEEEE		25.25-
447PhosphorylationGSDRLHMSLQQGKSS
CCCCCEEEECCCCCC		16.5719060867
453PhosphorylationMSLQQGKSSSTGNLL
EEECCCCCCCCCCCC		36.0227087446
454PhosphorylationSLQQGKSSSTGNLLD
EECCCCCCCCCCCCC		35.0923984901
455PhosphorylationLQQGKSSSTGNLLDK
ECCCCCCCCCCCCCH		47.6425521595
456PhosphorylationQQGKSSSTGNLLDKD
CCCCCCCCCCCCCHH		31.8527087446
466 (in isoform 4)Phosphorylation-25.6429514104
470 (in isoform 4)Phosphorylation-45.5826643407
472PhosphorylationLALPPPDYGTSSRAF
CCCCCCCCCCCCCCC		28.2525777480
472 (in isoform 4)Phosphorylation-28.2529899451
473 (in isoform 4)Phosphorylation-26.8825521595
474PhosphorylationLPPPDYGTSSRAFPT
CCCCCCCCCCCCCCC		19.8025777480
475 (in isoform 4)Phosphorylation-17.2926643407
475PhosphorylationPPPDYGTSSRAFPTQ
CCCCCCCCCCCCCCC		17.2925777480
476PhosphorylationPPDYGTSSRAFPTQT
CCCCCCCCCCCCCCC		27.7125777480
477 (in isoform 4)Phosphorylation-39.7626643407
480 (in isoform 4)Phosphorylation-23.7026643407
481 (in isoform 4)Phosphorylation-31.9025521595
486PhosphorylationFPTQTAGTFKQRPYS
CCCCCCCCCCCCCCC		25.7925521595
492PhosphorylationGTFKQRPYSVAVPAF
CCCCCCCCCEECCCC		20.2622817900
493PhosphorylationTFKQRPYSVAVPAFS
CCCCCCCCEECCCCC		13.2927087446
500O-linked_GlycosylationSVAVPAFSQGLDDYG
CEECCCCCCCCCCCC		25.9946232777
500PhosphorylationSVAVPAFSQGLDDYG
CEECCCCCCCCCCCC		25.99-
506 (in isoform 2)Phosphorylation-16.6129514104
506PhosphorylationFSQGLDDYGARSVSR
CCCCCCCCCCCCCCC		16.6122817900
510 (in isoform 2)Phosphorylation-24.7426643407
512 (in isoform 2)Phosphorylation-27.8229899451
513 (in isoform 2)Phosphorylation-53.3225521595
515 (in isoform 2)Phosphorylation-28.7226643407
517 (in isoform 2)Phosphorylation-20.5626643407
520 (in isoform 2)Phosphorylation-28.1326643407
521 (in isoform 2)Phosphorylation-6.5625521595
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of BAIP2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BAIP2_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of BAIP2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of BAIP2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BAIP2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453; SER-454 ANDSER-455, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND MASSSPECTROMETRY.

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